[Characterization of Cr (VI) removal and total Cr equilibrium adsorption by sulfate reducing granular sludge in stimulant wastewater].

Sulfate reducing granular sludge (SRGS) cultivated in small scale EGSB reactor was used for Cr (VI) removing. Characterization of Cr (VI) removal and total Cr equilibrium adsorption was studied, and the adsorption isotherm was fitted. Results showed that removal of Cr (VI) was in connection with the structure and chemical composition of SRGS and several environmental factors. The Cr (VI) removal rate increased with the dosage of granular sludge; the increasing of oscillation speed and temperature could enhance Cr (VI) removal and total Cr adsorption, but while the oscillation speed reached 150 r x min(-1) or the temperature came to 40 degrees C, the physical structure of granular sludge would be affected and the granular sludge discrete, and total Cr equilibrium adsorption decreased; lower pH value caused higher Cr (VI) removal rate, however the sulfate on the surface of granular sludge was affected by lower pH value easily and would translate into H2S, then total Cr adsorption rate decreased. Cr (VI) removal would be influenced by physical, chemical and biological factors, and the process included reduction and adsorption mainly. The maximum adsorption of total Cr by granular sludge was 6.84 mg x g(-1), and the total Cr adsorbing process fitted in with Langmuir adsorption isotherm.

Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state.

Inhibitor-2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase-1 (PP1), resulting in the formation of the inactive holoenzyme, ATP-Mg-dependent phosphatase. Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK-3 phosphorylation on the structure of free state I2[1-172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP-Mg-dependent phosphatase induced by GSK-3 phosphorylation must depend on the interactions between PP1 and I2.